Junctional adhesion molecule-like (JAML)

Junctional adhesion molecule-like (JAML) is a type I transmembrane protein from the immunoglobulin superfamily that localizes primarily at tight junctions of epithelial and endothelial cells, as well as on leukocytes[1][4]. It mediates **cell-cell adhesion** by homophilic and heterophilic interactions and regulates the **assembly of signal complexes** through its cytoplasmic PDZ-binding domains, scaffold proteins, and adjacent cell receptors[1]. JAML and related JAM family members are critical for leukocyte transmigration, immune surveillance, and the maintenance of tissue barrier function[1][4]. JAML interacts with integrins, modulates cell motility, and participates in the formation and stabilization of tight junctions, affecting cellular polarity and migration[1]. Its signaling functions are important for regulating leukocyte-endothelial interactions and epithelial integrity, and it may play roles in diseases that involve inflammation, immune cell trafficking, or barrier dysfunction[1][4]. JAML shares significant structural and functional homology with JAM-A, JAM-B, and JAM-C, but with specific tissue and cellular expression patterns[4]. There are no approved drugs targeting JAML directly, but its activity may be significant in contexts of inflammation, infection, or cancer where leukocyte trafficking and barrier stability are involved[1].

Other names

Junctional adhesion molecule-likeJAMLAMICA1AMICAUNQ722/PRO1387Gm638Adhesion molecule interacting with CXADR antigen 1Dendritic cell-specific protein CREA7-1CREA7-4adhesion molecule AMICAadhesion molecule, interacts with CXADR antigen 1

No approved drugs directly target JAML; mechanisms may involve modulation of cell adhesion, leukocyte migration, and barrier function if a drug did target this pathway.